Center for Heterocyclic Compounds, Department of Chemistry, University of Florida, Gainesville, FL 32611-7200, USA.
J Pept Sci. 2012 Nov;18(11):704-9. doi: 10.1002/psc.2438. Epub 2012 Oct 12.
S-Acyl cysteine peptides containing α-, β- or γ-amino acid residues undergo long-range S- to N-acyl transfer to give analogs of native tripeptides and tetrapeptides containing additional carbon atoms in the chain. The ease of intramolecular S → N-acyl transfer relative to intermolecular transacylation is favored increasingly for 9 < 12 < 13 ~ 10-membered cyclic transition states; the observed order is explained on conformational and intermolecular interaction considerations.
含 α-、β- 或 γ-氨基酸残基的 S-酰化半胱氨酸肽经历长程 S 到 N-酰基转移，生成含有链中额外碳原子的天然三肽和四肽类似物。对于 9 < 12 < 13~10 元环过渡态，分子内 S→N-酰基转移相对于分子间转酰基反应的容易程度增加；观察到的顺序可以用构象和分子间相互作用来解释。
